ASGL1_MACFA
ID ASGL1_MACFA Reviewed; 308 AA.
AC Q4R7U8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE EC=3.4.19.5 {ECO:0000250|UniProtKB:Q7L266};
DE EC=3.5.1.1 {ECO:0000250|UniProtKB:Q7L266};
DE AltName: Full=Asparaginase-like protein 1;
DE AltName: Full=Beta-aspartyl-peptidase;
DE AltName: Full=Isoaspartyl dipeptidase;
DE AltName: Full=L-asparagine amidohydrolase;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase alpha chain;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase beta chain;
DE Flags: Precursor;
GN Name=ASRGL1; ORFNames=QtsA-14329;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC May be involved in the production of L-aspartate, which can act as an
CC excitatory neurotransmitter in some brain regions. Is highly active
CC with L-Asp beta-methyl ester. Besides, has catalytic activity toward
CC beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-
CC L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala,
CC beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have
CC aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn.
CC Likewise, has no activity toward glutamine.
CC {ECO:0000250|UniProtKB:Q7L266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q7L266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266};
CC -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC autocleavage. This heterodimer may then dimerize in turn, giving rise
CC to a heterotetramer. {ECO:0000250|UniProtKB:Q7L266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}.
CC Note=Midpiece of sperm tail. {ECO:0000250|UniProtKB:Q7L266}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity.
CC {ECO:0000250|UniProtKB:Q7L266}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; AB168713; BAE00824.1; -; mRNA.
DR RefSeq; NP_001270754.1; NM_001283825.1.
DR RefSeq; XP_015289587.1; XM_015434101.1.
DR AlphaFoldDB; Q4R7U8; -.
DR SMR; Q4R7U8; -.
DR STRING; 9541.XP_005577653.1; -.
DR Ensembl; ENSMFAT00000027606; ENSMFAP00000002460; ENSMFAG00000036351.
DR GeneID; 101866084; -.
DR KEGG; mcf:101866084; -.
DR CTD; 80150; -.
DR VEuPathDB; HostDB:ENSMFAG00000036351; -.
DR eggNOG; KOG1592; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR OMA; YSRMRWK; -.
DR OrthoDB; 797598at2759; -.
DR Proteomes; UP000233100; Chromosome 14.
DR Bgee; ENSMFAG00000036351; Expressed in adult mammalian kidney and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; ISS:UniProtKB.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; ISS:UniProtKB.
DR GO; GO:0033345; P:asparagine catabolic process via L-aspartate; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04702; ASRGL1_like; 1.
DR InterPro; IPR033844; ASRGL1_meta.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..167
FT /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT /id="PRO_0000420557"
FT CHAIN 168..308
FT /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT /id="PRO_0000420558"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 196..199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219..222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7L266"
SQ SEQUENCE 308 AA; 32127 MW; 2071C67D472EAE89 CRC64;
MNPIVVVHGG GAGPISKDRK ERMHQGIVRA ATVGYGILRE GGSAVDAVEG AVVALEDDPE
FNAGCGSVLN TDGEVEMDAS IMDGKDLSVG AVSAVRCIAN PIKLARLVME KTPHCFLTDQ
GAAQFAAAMG VPEIPGEKLV TEKNKKRLEK EKHEKGAQKT DCEKNLGTVG AVALDFKGNV
AYATSTGGIV NKMVGRVGDT PCVGAGGYAD NDIGAISTTG HGESILKVNL ARLTLFHIEQ
GKTVEEAADL SLGYMKSRVK GLGGLIVVSK TGDWVAKWTS TSMPWAAAKD GKLHFGIDPD
DTAITDLP
